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A1AS76 (PUR9_PELPD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Bifunctional purine biosynthesis protein PurH

Including the following 2 domains:

  1. Phosphoribosylaminoimidazolecarboxamide formyltransferase
    EC=2.1.2.3
    Alternative name(s):
    AICAR transformylase
  2. IMP cyclohydrolase
    EC=3.5.4.10
    Alternative name(s):
    ATIC
    IMP synthase
    Inosinicase
Gene names
Name:purH
Ordered Locus Names:Ppro_2592
OrganismPelobacter propionicus (strain DSM 2379) [Complete proteome] [HAMAP]
Taxonomic identifier338966 [NCBI]
Taxonomic lineageBacteriaProteobacteriaDeltaproteobacteriaDesulfuromonadalesPelobacteraceaePelobacter

Protein attributes

Sequence length521 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

10-formyltetrahydrofolate + 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide = tetrahydrofolate + 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide. HAMAP-Rule MF_00139

Pathway

Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1. HAMAP-Rule MF_00139

Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1.

Domain

The IMP cyclohydrolase activity resides in the N-terminal region By similarity. HAMAP-Rule MF_00139

Sequence similarities

Belongs to the PurH family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 521521Bifunctional purine biosynthesis protein PurH HAMAP-Rule MF_00139
PRO_1000057903

Sequences

Sequence LengthMass (Da)Tools
A1AS76 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 0DE49052151DD7E2

FASTA52156,449
        10         20         30         40         50         60 
MAKIKRALIS VSNKRGIIEF SKVLAGYGVE ILSTGGTAKL LRDSGVDVKD VSEFTGFPEM 

        70         80         90        100        110        120 
LDGRVKTLHP KVHGGLLGMR GNPEHVAKMR EFGIENIDMV VVNLYPFEAT VAKEGCLLVD 

       130        140        150        160        170        180 
AIENIDIGGP TMLRSAAKNY PDVTVLVDSV DYATIVDEMR ENGGEVSAKT NFGLAVKAFQ 

       190        200        210        220        230        240 
HTAAYDGAIS NYLGARLGEG VDPFPPTFTF QVRKSQELRY GENPQQSAAF YVERDQHEAS 

       250        260        270        280        290        300 
VATCHQIQGK ELSYNNIADT DAALECVKQF TEGPTCVIVK HANPCGVAIG SSLLEAYDRA 

       310        320        330        340        350        360 
YSTDPESAFG GIIACNRELD LETARAICER QFVEVIVAPT ASPEAVQVVS SKKNVRLLVY 

       370        380        390        400        410        420 
GEWPQTVVPR LDFKRVTGGL LVQSADQELF KNLQVVTKRQ PTPEELIDLQ FSWRVAKFVK 

       430        440        450        460        470        480 
SNAIVYGRDG MTIGVGAGQM SRVNSARIAA IKAEHAGLVV EGAVMASDAF FPFRDGIDNA 

       490        500        510        520 
ASVGIRAVIQ PGGSMRDAEV IAAADEHGMA MVFTGMRHFR H 

« Hide

References

[1]"Complete sequence of chromosome of Pelobacter propionicus DSM 2379."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J., Larimer F. expand/collapse author list , Land M., Hauser L., Kyrpides N., Kim E., Lovley D., Richardson P.
Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2379.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000482 Genomic DNA. Translation: ABL00197.1.
RefSeqYP_902254.1. NC_008609.1.

3D structure databases

ProteinModelPortalA1AS76.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING338966.Ppro_2592.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABL00197; ABL00197; Ppro_2592.
GeneID4572925.
KEGGppd:Ppro_2592.
PATRIC22898281. VBIPelPro64470_2746.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0138.
HOGENOMHOG000230372.
KOK00602.
OMARAFKTDP.
OrthoDBEOG6QCDFF.

Enzyme and pathway databases

BioCycPPRO338966:GHL0-2633-MONOMER.
UniPathwayUPA00074; UER00133.
UPA00074; UER00135.

Family and domain databases

Gene3D3.40.140.20. 2 hits.
3.40.50.1380. 1 hit.
HAMAPMF_00139. PurH.
InterProIPR024051. AICAR_Tfase_dom.
IPR002695. AICARFT_IMPCHas.
IPR016193. Cytidine_deaminase-like.
IPR011607. MGS-like_dom.
[Graphical view]
PANTHERPTHR11692. PTHR11692. 1 hit.
PfamPF01808. AICARFT_IMPCHas. 1 hit.
PF02142. MGS. 1 hit.
[Graphical view]
PIRSFPIRSF000414. AICARFT_IMPCHas. 1 hit.
SMARTSM00798. AICARFT_IMPCHas. 1 hit.
SM00851. MGS. 1 hit.
[Graphical view]
SUPFAMSSF52335. SSF52335. 1 hit.
SSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR00355. purH. 1 hit.
ProtoNetSearch...

Entry information

Entry namePUR9_PELPD
AccessionPrimary (citable) accession number: A1AS76
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways